Exploring the binding interaction between copper ions and Candida rugosa lipase.

ABSTRACT: The wide range of applications of copper have caused widespread concern about its toxicity. However, few studies have reported the mechanism of the binding interaction between copper ions and digestive enzymes, which play an important role in physiological health and industrial production. In this study, the effects of copper ions on the conformation and activity of Candida rugosa lipase (CRL) were evaluated by isothermal titration calorimetry (ITC), multiple spectral techniques, molecular simulation and enzyme activity assays. The results showed that copper ions can be combined with lipase, the binding affinity constant (K) was (2.91 ± 0.619) × 10^-3 M^-1, the binding process was a spontaneous process, and the main force was the hydrophobic force. Rather than in

SUBMITTER: Qu W 

PROVIDER: S-EPMC6249630 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature